An odorant receptor tuned to an attractive plant volatile vanillin in Spodoptera litura.
Molecular docking
Oviposition preference
The common cutworm
Two-electrode voltage clamp recording
Xenopus oocyte
Y-tube olfactometer
Journal
Pesticide biochemistry and physiology
ISSN: 1095-9939
Titre abrégé: Pestic Biochem Physiol
Pays: United States
ID NLM: 1301573
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
11
08
2023
revised:
02
09
2023
accepted:
11
09
2023
medline:
13
11
2023
pubmed:
10
11
2023
entrez:
9
11
2023
Statut:
ppublish
Résumé
The insect olfaction plays crucial roles in many important behaviors, in which ORs are key determinants for signal transduction and the olfactory specificity. Spodoptera litura is a typical polyphagous pest, possessing a large repertoire of ORs tuning to broad range of plant odorants. However, the specific functions of those ORs remain mostly unknown. In this study, we functionally characterized one S. litura OR (OR51) that was highly expressed in the adult antennae. First, by using Xenopus oocyte expression and two-electrode voltage clamp recording system (XOE-TEVC), OR51 was found to be strongly and specifically responsive to vanillin (a volatile of S. litura host plants) among 77 tested odorants. Second, electroantennogram (EAG) and Y-tube behavioral experiment showed that vanillin elicited significant EAG response and attraction behavior especially of female adults. This female attraction was further confirmed by the oviposition experiment, in which the soybean plants treated with vanillin were significantly preferred by females for egg-laying. Third, 3D structural modelling and molecular docking were conducted to explore the interaction between OR51 and vanillin, which showed a high affinity (-4.46 kcal/mol) and three residues (Gln163, Phe164 and Ala305) forming hydrogen bonds with vanillin, supporting the specific binding of OR51 to vanillin. In addition, OR51 and its homologs from other seven noctuid species shared high amino acid identities (78-97%) and the same three hydrogen bond forming residues, suggesting a conserved function of the OR in these insects. Taken together, our study provides some new insights into the olfactory mechanisms of host plant finding and suggests potential applications of vanillin in S. litura control.
Identifiants
pubmed: 37945255
pii: S0048-3575(23)00284-5
doi: 10.1016/j.pestbp.2023.105619
pii:
doi:
Substances chimiques
Receptors, Odorant
0
vanillin
CHI530446X
Insect Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105619Informations de copyright
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